title: Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies.
abstract: Dual binding modes: Combined empirical and computational studies of a series of compounds showed adenine and 1-benzyl-4-(dimethylamino)pyridinium fragments to function most efficiently in binding CHOKα1, and also determined how the latter fragment interacts with the choline binding site through two different binding modes. These data provide a basis for the future design of better and more selective inhibitors.
authors.affiliation: Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D, 50018 Zaragoza, Spain.
authors.forename: María
authors.initials: M
authors.lastname: Sahún-Roncero
authors.forename: Belén
authors.initials: B
authors.lastname: Rubio-Ruíz
authors.forename: Ana
authors.initials: A
authors.lastname: Conejo-García
authors.forename: Adrián
authors.initials: A
authors.lastname: Velázquez-Campoy
authors.forename: Antonio
authors.initials: A
authors.lastname: Entrena
authors.forename: Ramon
authors.initials: R
authors.lastname: Hurtado-Guerrero
mesh_terms: D000225:Adenine / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D020134:Catalytic Domain; D002797:Choline Kinase / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D062105:Molecular Docking Simulation; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
chemical_list: D002797:Choline Kinase; D000225:Adenine
keywords: CHOKalpha1 and CHOKbeta; X-ray crystallography; cancer; chemical deconvolution; ligand design; protein structures